2A8F

beta-cinnamomin after sterol removal

Summary for 2A8F

• Entry DOI: 10.2210/pdb2a8f/pdb
• Descriptor: Beta-elicitin cinnamomin (2 entities in total)
• Functional Keywords: elicitin, sterol carrier protein, phytophthora, phytopathogen, toxin
• Biological source: Phytophthora cinnamomi
• Cellular location: Secreted: P15569
• Total number of polymer chains: 2
• Total formula weight: 20599.52

Authors

Rodrigues, M.L.,Archer, M.,Martel, P.,Miranda, S.,Thomaz, M.,Enguita, F.J.,Baptista, R.P.,Melo, E.P.,Sousa, N.,Cravador, A.,Carrondo, M.A. (deposition date: 2005-07-08, release date: 2006-01-17, Last modification date: 2024-10-09)

Primary citation

Rodrigues, M.L.,Archer, M.,Martel, P.,Miranda, S.,Thomaz, M.,Enguita, F.J.,Baptista, R.P.,Melo, E.P.,Sousa, N.,Cravador, A.,Carrondo, M.A.
Crystal structures of the free and sterol-bound forms of beta-cinnamomin
Biochim.Biophys.Acta, 1764:110-121, 2006

PubMed Abstract: The crystal structure of the elicitin beta-cinnamomin (beta-CIN) was determined in complex with ergosterol at 1.1 A resolution. beta-CIN/ergosterol complex crystallized in the monoclinic space group P2(1), with unit cell parameters of a = 31.0, b = 62.8, c = 50.0 A and beta = 93.4 degrees and two molecules in the asymmetric unit. Ligand extraction with chloroform followed by crystallographic analysis yielded a 1.35 A structure of beta-CIN (P4(3)2(1)2 space group) where the characteristic elicitin fold was kept. After incubation with cholesterol, a new complex structure was obtained, showing that the protein retains, after the extraction procedure, its ability to complex sterols. The necrotic effect of beta-CIN on tobacco was also shown to remain unchanged. Theoretical docking studies of the triterpene lupeol to beta-CIN provided an explanation for the apparent inability of beta-CIN to bind this ligand, as observed experimentally.

PubMed: 16249127
DOI: 10.1016/j.bbapap.2005.09.008

Experimental method

X-RAY DIFFRACTION (1.35 Å)